Novel structural insights into F-actin-binding and novel functions of calponin homology domains.
Tandem calponin homology (CH) domains are well-known actin filaments (F-actin) binding motifs. There has been a continuous debate about the details of CH domain-actin interaction, mainly because atomic level structures of F-actin are not available. A recent electron microscopy study has considerably advanced our structural understanding of CH domain:F-actin complex. On the contrary, it has recently also been shown that CH domains can bind other macromolecular systems: two CH domains from separate polypeptides Ncd80, Nuf2 can form a microtubule-binding site, as well as tandem CH domains in the EB1 dimer, while the single C-terminal CH domain of alpha-parvin has been observed to bind to a alpha-helical leucin-aspartate rich motif from paxillin.
Sjöblom
Björn
B
Department for Biomolecular Structural Chemistry, Max F. Perutz Laboratories, University of Vienna, Campus Vienna Biocenter 5, A-1030 Vienna, Austria.
Ylänne
Jari
J
Djinović-Carugo
Kristina
K
D008841:Actin Cytoskeleton / Q000378:metabolism; D000199:Actins / Q000737:chemistry* / Q000378:metabolism*; D002135:Calcium-Binding Proteins / Q000737:chemistry* / Q000378:metabolism*; D008840:Microfilament Proteins / Q000737:chemistry* / Q000378:metabolism*; D008854:Microscopy, Electron; D008870:Microtubules / Q000378:metabolism; D051419:Paxillin / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding; D054730:Protein Interaction Domains and Motifs; D040681:Structural Homology, Protein; D000096985:Calponins
D000199:Actins; D002135:Calcium-Binding Proteins; D008840:Microfilament Proteins; D051419:Paxillin; D000096985:Calponins